The DOI matches its Crossref record; 59 of the 59 references it cites were found in a registry or an index.
J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth.
Open accessAbstract
The influence of J1/tenascin adsorbed to polyornithine-conditioned plastic (substrate-bound J1/tenascin) and J1/tenascin present in the culture medium (soluble J1/tenascin) on neurite outgrowth was studied with cultured single cells from hippocampus and mesencephalon of embryonic rats. Neurons at low density grew well on J1/tenascin substrates and extended neurites that were approximately 40% longer than on the polyornithine control substrate after 24 h in vitro. The neurite outgrowth promoting effect of substrate bound J1/tenascin was largely abolished in the presence of mAb J1/tn2, but not by mAb J1/tn1. In contrast to the neurite growth-promoting effects of substrate bound J1/tenascin, neurite outgrowth on polyornithine, laminin, fibronectin, or J1/tenascin as substrates was inhibited by addition of soluble J1/tenascin to the cultures. Neither of the two mAbs neutralized the neurite outgrowth-inhibitory properties of soluble J1/tenascin. In contrast to their opposite effects on neurite outgrowth, both substrate-bound and soluble J1/tenascin reduced spreading of the neuronal cell bodies, suggesting that the neurite outgrowth-promoting and antispreading effects are mediated by two different sites on the molecule. This was further supported by the inability of the mAb J1/tn2 to neutralize the antispreading effect. The J1/tn2 epitope localizes to a fibronectin type III homology domain that is presumably distinct from the putative Tn68 cell-binding domain of chicken tenascin for fibroblasts, as shown by electronmicroscopic localization of antibody binding sites. We infer from these experiments that J1/tenascin contains a neurite outgrowth promoting domain that is distinguishable from the cell-binding site and presumably not involved in the inhibition of neurite outgrowth or cell spreading. Our observations support the notion that J1/tenascin is a multifunctional extracellular matrix molecule.
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Self-citationTenascin: An Extracellular Matrix Protein Prominent in Specialized Embryonic Tissues and Tumors
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The cellular and molecular basis of peripheral nerve regeneration
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Metadata
- Authors
- Lochter, A., Vaughan, L., Kaplony, A., Prochiantz, A., Schachner, M., & Faissner, A.
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1991-06-01
- Volume
- 113
- Issue
- 5
- Pages
- 1159-1171
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2038303772
- Cited by
- 275
- References
- 59
- FWCI
- 8.87
- Type
- journal article
- Language
- en
- Open access
- green
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- Lochter, A., Vaughan, L., Kaplony, A., Prochiantz, A., Schachner, M., & Faissner, A. (1991). J1/tenascin in substrate-bound and soluble form displays contrary effects on neurite outgrowth. The Journal of cell biology. https://doi.org/10.1083/jcb.113.5.1159
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